ORGN 731 |
| To better understand and control β-sheet interactions between disease-related proteins, our research group is developing chemical models of protein β-sheets. This poster describes the development of 54-membered-ring cyclic peptides that fold and dimerize in water through interchain β-sheet interactions. These cyclic peptides, which contain two unnatural amino acids Hao on one edge and a heptapeptide β-strand on the other edge, form β-sheet dimers that further associate to form higher oligomers, possibly tetramers.
|
|
Asymmetric Reactions, Molecular Recognition, Self Assembly, Bioorganic Chemistry, Process R&D
8:00 PM-10:00 PM, Wednesday, 16 March 2005 Convention Center -- Hall D, Poster
Division of Organic Chemistry |
